ID G1KT60_ANOCA Unreviewed; 663 AA.
AC G1KT60;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Poly(ADP-ribose) polymerase family member 12 {ECO:0000313|Ensembl:ENSACAP00000016560.3};
GN Name=PARP12 {ECO:0000313|Ensembl:ENSACAP00000016560.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000016560.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000016560.3, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000016560.3,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000016560.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
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DR RefSeq; XP_003220925.1; XM_003220877.3.
DR AlphaFoldDB; G1KT60; -.
DR STRING; 28377.ENSACAP00000016560; -.
DR Ensembl; ENSACAT00000016886.4; ENSACAP00000016560.3; ENSACAG00000016815.4.
DR GeneID; 100561568; -.
DR KEGG; acs:100561568; -.
DR eggNOG; ENOG502QSC4; Eukaryota.
DR GeneTree; ENSGT00940000154649; -.
DR HOGENOM; CLU_014825_2_1_1; -.
DR InParanoid; G1KT60; -.
DR OrthoDB; 5490222at2759; -.
DR TreeFam; TF338389; -.
DR Proteomes; UP000001646; Chromosome 5.
DR Bgee; ENSACAG00000016815; Expressed in dewlap and 12 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; IEA:Ensembl.
DR CDD; cd01439; TCCD_inducible_PARP_like; 1.
DR Gene3D; 3.30.1370.210; -; 1.
DR Gene3D; 3.30.720.50; -; 1.
DR Gene3D; 3.90.228.10; -; 1.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR037197; WWE_dom_sf.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR45740; POLY [ADP-RIBOSE] POLYMERASE; 1.
DR PANTHER; PTHR45740:SF6; PROTEIN MONO-ADP-RIBOSYLTRANSFERASE PARP12; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00356; ZnF_C3H1; 3.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50918; WWE; 1.
DR PROSITE; PS50103; ZF_C3H1; 3.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT DOMAIN 95..120
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 181..203
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 260..287
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 354..441
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 470..663
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT ZN_FING 95..120
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 181..203
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 260..287
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 238..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 76039 MW; 6F4C9C49AB3C0D5E CRC64;
MLSTSSSRIY KELCASGGSL SEDELGRRLG LQGRAGLLAQ LLQDASKFTL VTREEPPSSA
ASGGESRTVV AKTGARLCAQ HGSGKCQGDC RQLHLCRFFV YGACRHQGTR KQCRFIHDFY
SPCNLAVLKE HELEKLSSDD LCQLLLQNDP SLLPEVCAYY NKGDGPYGSC NFKKICVKLH
ICQYYLHGDC RFGSNCKRSH DVFNPDCYEK LEKWGMTRAL ITRIPLIYRN AYDIRNSTPS
PCKERRESSS QVPSTTNSID ESDTICLYYI RKSCSFQDKC IRVHFHLPYR WQTLDGAQWK
DLANMEKIEQ DYCDPFHERM VYNGLGNDSK VLVIDFSNMT CNSAKLRRLS TASSVTKAPY
YILTTDWIWY WKDECDVWNE YGVKDLDHDA ATLSSFDLEK AYQSEASPTL KFSAGKHTYE
LDFRVMKQKN LRYLTERSIR RRPKFVSPKE VEEKKKTGGV AQSKGGTALI PAHWDQSALP
ELGYTLVTLL SSSNEYRKVQ VNFQRTMPKA TIVEIKRIQN RALWEVYQWQ KEQMKKANDG
KDVDERQLFH GTNKSHVDAI CQQNFDWRIC GVHGTAYGKG SYFARDASYS DNYSDSTNKI
MFLARVLVGE FTIGMSSYLR PPQKEVQSTG FYNSCVNDLR NPSIFVIFEK HQIYPEYVIK
YRN
//
